RT Journal Article
T1 Urea equilibrium unfolding of the major core protein of the  retrovirus feline immunodeficiency virus and its tryptophan  mutants
A1 Yélamos, Belén
A1 Núñez, Elena
A1 Gómez Gutiérrez, Julián
A1 Delgado, Carmen
A1 Pacheco González, Beatriz
A1 Peterson, Darrell L.
A1 Gavilanes, Francisco
AB Circular dichroism and fluorescence spectroscopy have been employed to study the urea unfolding mechanism of a recombinant form of the major core protein of feline immunodeficiency virus (FIV-rp24) and its native tryptophan mutants. The equilibrium denaturation curves indicate the existence of two transitions. The first unfolding transition most likely reflects the denaturation of the carboxy-terminal region of FIV-rp24. Consequently, the second transition, where the changes in fluorescence are produced, should reflect the denaturation of the amino-terminal region. If the intermediate observed upon urea denaturation is an on- pathway species, the data described herein can reflect the sequential and independent loss of structure of the two domains that this type of proteins possesses.
PB ELSEVIER SCIENCE BV
SN 0167-4838
YR 2001
FD 2001-03-09
LK https://hdl.handle.net/20.500.14352/59749
UL https://hdl.handle.net/20.500.14352/59749
LA eng
NO Yélamos, B., Núñez, E., Gómez Gutiérrez, J. et al. «Urea Equilibrium Unfolding of the Major Core Protein of the Retrovirus Feline Immunodeficiency Virus and Its Tryptophan Mutants». Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, vol. 1546, n.o 1, marzo de 2001, pp. 87-97. DOI.org (Crossref), https://doi.org/10.1016/S0167-4838(00)00300-9.
NO Dirección General de Enseñanza Superior (España)
NO Institutos Nacionales de Salud (Estados Unidos)
DS Docta Complutense
RD 11 abr 2025